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Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach
The molecular dynamic (MD) modeling approach was applied to evaluate the effect of an external electric field on soybean hydrophobic protein and surface properties. Nominal electric field strengths of 0.002 V/nm and 0.004 V/nm had no major effect on the structure and surface properties of the protei...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4030879/ https://www.ncbi.nlm.nih.gov/pubmed/24970163 http://dx.doi.org/10.3390/biom3010168 |
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author | Singh, Ashutosh Orsat, Valérie Raghavan, Vijaya |
author_facet | Singh, Ashutosh Orsat, Valérie Raghavan, Vijaya |
author_sort | Singh, Ashutosh |
collection | PubMed |
description | The molecular dynamic (MD) modeling approach was applied to evaluate the effect of an external electric field on soybean hydrophobic protein and surface properties. Nominal electric field strengths of 0.002 V/nm and 0.004 V/nm had no major effect on the structure and surface properties of the protein isolate but the higher electric field strength of 3 V/nm significantly affected the protein conformation and solvent accessible surface area. The response of protein isolate to various external field stresses demonstrated that it is necessary to gain insight into protein dynamics under electromagnetic fields in order to be able to develop the techniques utilizing them for food processing and other biological applications. |
format | Online Article Text |
id | pubmed-4030879 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-40308792014-06-24 Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach Singh, Ashutosh Orsat, Valérie Raghavan, Vijaya Biomolecules Article The molecular dynamic (MD) modeling approach was applied to evaluate the effect of an external electric field on soybean hydrophobic protein and surface properties. Nominal electric field strengths of 0.002 V/nm and 0.004 V/nm had no major effect on the structure and surface properties of the protein isolate but the higher electric field strength of 3 V/nm significantly affected the protein conformation and solvent accessible surface area. The response of protein isolate to various external field stresses demonstrated that it is necessary to gain insight into protein dynamics under electromagnetic fields in order to be able to develop the techniques utilizing them for food processing and other biological applications. MDPI 2013-02-11 /pmc/articles/PMC4030879/ /pubmed/24970163 http://dx.doi.org/10.3390/biom3010168 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Singh, Ashutosh Orsat, Valérie Raghavan, Vijaya Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach |
title | Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach |
title_full | Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach |
title_fullStr | Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach |
title_full_unstemmed | Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach |
title_short | Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach |
title_sort | soybean hydrophobic protein response to external electric field: a molecular modeling approach |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4030879/ https://www.ncbi.nlm.nih.gov/pubmed/24970163 http://dx.doi.org/10.3390/biom3010168 |
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